Výsledky vyhledávání - "Victor Adler"

The anti-cancer peptide, PNC-27, induces tumor cell lysis as the intact peptide

Autor: Victor Adler, Wilbur B. Bowne, Matthew R. Pincus, Josef Michl, Ehsan Sarafraz-Yazdi, Kelley A. Sookraj

Publikováno v: Cancer Chemotherapy and Pharmacology. 66:325-331

PNC-27, a peptide that contains an HDM-2-binding domain from p53 attached to a membrane-penetrating peptide on its carboxyl terminal end, is cytotoxic to cancer, but not normal, cells. It forms transmembrane pores in the cancer cell membrane. Our pur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32ea5382680f1ef646d98a09695c8b92
https://doi.org/10.1007/s00280-009-1166-7

Zobrazit plný text záznamu

The Penetratin Sequence in the Anticancer PNC-28 Peptide Causes Tumor Cell Necrosis Rather Than Apoptosis of Human Pancreatic Cancer Cells

Autor: Mou Ng, Victor Adler, Michael E. Zenilman, Kelley A. Sookraj, Kamran Ikram, Martin H. Bluth, Wilbur B. Bowne, Stephan Bradu, Sunming Lou, Raqibul Hannan, Jesco Koenke, Ehsan Sarafraz-Yazdi, Josef Michl, Michael Harding, Michael Vishnevetsky, Vadim Shteyler, Matthew R. Pincus, Paul W. Brandt-Rauf

Publikováno v: Annals of Surgical Oncology. 15:3588-3600

PNC-27 and PNC-28 are p53-derived peptides from the human double minute (hdm-2) binding domain attached to penetratin. These peptides induce tumor cell necrosis of cancer cells, but not normal cells. The anticancer activity and mechanism of PNC-28 (p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f413605f7dc21f4b3168b87321452674
https://doi.org/10.1245/s10434-008-0147-0

Zobrazit plný text záznamu

Two peptides derived from ras-p21 induce either phenotypic reversion or tumor cell necrosis of ras-transformed human cancer cells

Autor: Josef Michl, Matthew R. Pincus, Ikram Kamran, Wilbur B. Bowne, Fred K. Friedman, Michael E. Zenilman, Edwin Chin, Victor Adler

Publikováno v: Cancer Chemotherapy and Pharmacology. 62:491-498

We investigated the effects of two peptides from the ras-p21 protein, corresponding to residues 35–47 (PNC-7) and 96–110 (PNC-2), on two ras-transformed human cancer cell lines, HT1080 fibrosarcoma and MIAPaCa-2 pancreatic cancer cell lines. In p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48d39179795056e828d188c6ffd7e3d3
https://doi.org/10.1007/s00280-007-0630-5

Zobrazit plný text záznamu

Small, Highly Structured RNAs Participate in the Conversion of Human Recombinant PrPSen to PrPRes in Vitro

Autor: Valentin Kryukov, Brian Zeiler, Richard Rubenstein, Richard J. Kascsak, Victor Adler, Abraham Grossman

Publikováno v: Journal of Molecular Biology. 332:47-57

We have identified a small, highly structured (shs)RNA that binds human recombinant prion protein (hrPrP) with high affinity and specificity under physiological conditions (e.g. 10% bovine calf serum (BCS), neutral pH, nanomolar concentrations of RNA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bafa553cd97e768a21991144d6f22e8c
https://doi.org/10.1016/s0022-2836(03)00919-7

Zobrazit plný text záznamu

The anti-cancer peptide, PNC-27, induces tumor cell necrosis of a poorly differentiated non-solid tissue human leukemia cell line that depends on expression of HDM-2 in the plasma membrane of these cells

Autor: Katlin, Davitt, Blake D, Babcock, Maly, Fenelus, Chi Kong, Poon, Abhishek, Sarkar, Vincent, Trivigno, Paul A, Zolkind, Sheena M, Matthew, Natalia, Grin'kina, Zulfiya, Orynbayeva, Mohammad F, Shaikh, Victor, Adler, Josef, Michl, Ehsan, Sarafraz-Yazdi, Matthew R, Pincus, Wilbur B, Bowne

Publikováno v: Annals of clinical and laboratory science. 44(3)

We have developed the anti-cancer peptide, PNC-27, which is a membrane-active peptide that binds to the HDM-2 protein expressed in the cancer cell membranes of solid tissue tumor cells and induces transmembrane pore formation in cancer, but not in no

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b326c6945c50f6a6049a355083abc44a
https://pubmed.ncbi.nlm.nih.gov/25117093

Zobrazit plný text záznamu

Induction of oocyte maturation by jun -N-terminal kinase (JNK) on the oncogenic ras -p21 pathway is dependent on the raf -MEK-MAP kinase signal transduction pathway

Autor: S. Amar, Josef Michl, Ziro Yamaizumi, Cecilia Kovac, M. C. M. Lin, Ze'ev Ronai, Victor Adler, Matthew R. Pincus, Fred K. Friedman, Denise L. Chung, H.-F. Kung, Lyndon Chie, Richard C. Robinson, H. Chen, Paul W. Brandt-Rauf

Publikováno v: Cancer Chemotherapy and Pharmacology. 45:441-449

Purpose: We have previously found that microinjection of activated MEK (mitogen activated kinase kinase) and ERK (mitogen-activated protein; MAP kinase) fails to induce oocyte maturation, but that maturation, induced by oncogenic ras-p21 and insulin-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fce60fea57f94046cdff10210b4471a
https://doi.org/10.1007/s002800051017

Zobrazit plný text záznamu

Analysis of JNK, Mdm2 and p14ARF contribution to the regulation of mutant p53 stability

Autor: Serge Y. Fuchs, Victor Adler, Toshinari Minamoto, Thomas Buschmann, Ze'ev Ronai, Nikhil Wagle, Masyoshi Mai

Publikováno v: Journal of Molecular Biology. 295:1009-1021

Identification of Mdm2 and JNK as proteins that target degradation of wt p53 prompted us to examine their effect on mutant p53, which exhibits a prolonged half-life. Of five mutant p53 forms studied for association with the targeting molecules, two n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4b1c050cf63a2e11d2a10e1f5f3a2fc
https://doi.org/10.1006/jmbi.1999.3387

Zobrazit plný text záznamu

JNK targets p53 ubiquitination and degradation in nonstressed cells

Autor: Zhimin Yin, Ze'ev Ronai, Stephen N. Jones, Serge Y. Fuchs, Thomas Buschmann, Victor Adler, Xiangwei Wu

Publikováno v: Scopus-Elsevier

In this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount of p53–JNK complex was inversely correlated with p53 level. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dafe6fb064db2678d3082b2022ce83f1
https://doi.org/10.1101/gad.12.17.2658

Zobrazit plný text záznamu

c-Jun NH2-terminal Kinases Target the Ubiquitination of Their Associated Transcription Factors

Autor: Victor A. Fried, Victor Adler, Bin Xie, Serge Y. Fuchs, Ze'ev Ronai, Roger J. Davis

Publikováno v: Journal of Biological Chemistry. 272:32163-32168

Regulatory proteins are often ubiquitinated, depending on their phosphorylation status as well as on their association with ancillary proteins that serve as adapters of the ubiquitination machinery. We previously demonstrated that c-Jun is targeted f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a5d89ef3985e25b28c197a9b385969
https://doi.org/10.1074/jbc.272.51.32163

Zobrazit plný text záznamu

Conformation-dependent phosphorylation of p53

Autor: Victor Adler, Fred K. Friedman, Curtis C. Harris, Toshinari Minamoto, Mark J. Bluth, James M. Chen, Xin Wei Wang, Paul W. Brandt-Rauf, Serge Y. Fuchs, Matthew R. Pincus, Richard C. Robinson, Ze'ev Ronai

Publikováno v: Proceedings of the National Academy of Sciences. 94:1686-1691

Phosphorylation of the p53 tumor suppressor protein is known to modulate its functions. Using bacterially produced glutathione S -transferase (GST)-p53 fusion protein and baculovirus-expressed histidine-tagged p53 ( His p53), we have determined human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f0eecc36a7d15bb15dfcfa8b193855e
https://doi.org/10.1073/pnas.94.5.1686

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání